کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5402443 | 1392734 | 2010 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Spectroscopic studies on the interaction between disperse blue SBL and bovine serum albumin
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی تئوریک و عملی
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چکیده انگلیسی
The interaction of disperse blue SBL (DBSBL) with bovine serum albumin (BSA) was investigated using fluorescence, UV-visible and far-UV circular dichroism (CD) spectroscopy. The results showed that the fluorescence of BSA was quenched by DBSBL through static quenching after correcting for the inner filter effects (IFE). The binding constant Kb of DBSBL with BSA at 288, 298 and 303Â K were 0.116Ã106, 3.18Ã106 and 12.3Ã106Â LÂ molâ1, respectively. The thermodynamic parameters, standard enthalpy change (ÎH0) and standard entropy change (ÎS0), for the reaction were evaluated to be 227.2Â kJÂ molâ1 and 886Â JÂ molâ1Â Kâ1 according to the van't Hoff equation. The above data suggested that the forces acting between DBSBL and BSA were predominantly hydrophobic interactions. The results of UV-visible absorption and far-UV CD spectroscopy also revealed that the conformation and microenvironment of BSA molecule were changed after DBSBL binding to BSA. At 288Â K one binding site was present but at higher temperatures a second binding site was detected between DBSBL and the BSA molecule. The lower bound for the distance between the bound dye and the Trp residue is 2.35Â nm as calculated from Forster energy transfer.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Luminescence - Volume 130, Issue 8, August 2010, Pages 1384-1389
Journal: Journal of Luminescence - Volume 130, Issue 8, August 2010, Pages 1384-1389
نویسندگان
Yumei Guo, Qinyan Yue, Baoyu Gao, Qianqian Zhong,